David M. Mofford

TL;DR: Firefly luciferase can be mutated to accept and utilize rigid aminoluciferins with high activity in both live and lysed cells yet exhibit 10 000-fold selectivity over the natural Luciferase substrate, paving the way to an extended family of bioluminescent reporters.

TL;DR: Firefly luciferase substrate d-luciferin and its analogs are fatty acid mimics that are ideally suited to probe the chemistry of enzymes that release fatty acid products and serve as exemplary reagents for greatly improved bioluminescence imaging in FAAH-expressing tissues such as the brain.

TL;DR: The creation of mutant luciferases that yield improved sustained light emission with aminoluciferins in both lysed and live mammalian cells, allowing the use of aminolucifierins for cell-based bioluminescence experiments.

TL;DR: It is shown that mutants of firefly luciferase can discriminate between natural and synthetic substrates in the brains of live mice and that mutant luciferases that are inactive or weakly active with d-luciferin can light up brightly when treated with the aminoluciferins CycLuc1 and Cyc Luc2 or their respective FAAH-sensitive luciferin amides.

TL;DR: The Drosophila fatty acyl-CoA synthetase CG6178, which cannot use d-luciferin as a substrate, is able to catalyze light emission from the synthetic luciferin analog CycLuc2, expanding the scope of bioluminescence and demonstrating that the introduction of a new substrate can unmask latent enzymatic activity that differs significantly from an enzyme’s normal function without requiring mutation.